Identification of a reversible structural transition in the metal-depleted glycerol dehydrogenase from Bacillus stearothermophilus.
Evidence is presented to demonstrate that the Zn2+ -depleted, inactive form of the glycerol dehydrogenase from Bacillus stearothermophilus exists in one of two possible conformations in equilibrium, the position of which is temperature sensitive. The conformation of the metal-depleted enzyme favoured by higher temperatures (20-40 degrees C) is able to bind Zn2+ and regain catalytic activity, whereas that favoured at lower temperatures (0-10 degrees C) is unable to bind metal ions and is thus inactive. This equilibrium is also pH dependent with a pK of 6.6. At pH 6.0, the equilibrium lies in favour of the form of the enzyme able to bind metal ions and exhibit activity.
Spencer
P
P
Department of Biochemistry, School of Biochemical and Physiological Sciences, University of Southampton, England.
Paine
L J
LJ
Scawen
M D
MD
Atkinson
T
T
Gore
M G
MG
D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008667:Metalloproteins / Q000378:metabolism*; D011487:Protein Conformation; D013401:Sugar Alcohol Dehydrogenases / Q000378:metabolism*; D013816:Thermodynamics; D015032:Zinc / Q000378:metabolism*
D008667:Metalloproteins; D013401:Sugar Alcohol Dehydrogenases; C020672:glycerol dehydrogenase; D015032:Zinc